4i3a: Difference between revisions
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==Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS== | ==Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS== | ||
<StructureSection load='4i3a' size='340' side='right' caption='[[4i3a]], [[Resolution|resolution]] 1.60Å' scene=''> | <StructureSection load='4i3a' size='340' side='right'caption='[[4i3a]], [[Resolution|resolution]] 1.60Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4i3a]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[4i3a]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Halorhodospira_halophila Halorhodospira halophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4I3A OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4I3A FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=HC4:4-HYDROXYCINNAMIC+ACID'>HC4</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4i3a FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4i3a OCA], [https://pdbe.org/4i3a PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4i3a RCSB], [https://www.ebi.ac.uk/pdbsum/4i3a PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4i3a ProSAT]</span></td></tr> | |||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/PYP_HALHA PYP_HALHA] Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Halorhodospira halophila]] | ||
[[Category: Ihee | [[Category: Large Structures]] | ||
[[Category: Jung | [[Category: Ihee H]] | ||
[[Category: Kim | [[Category: Jung YO]] | ||
[[Category: Lee | [[Category: Kim J]] | ||
[[Category: Moffat | [[Category: Lee JH]] | ||
[[Category: Schmidt | [[Category: Moffat K]] | ||
[[Category: Vukica | [[Category: Schmidt M]] | ||
[[Category: Vukica S]] | |||
Latest revision as of 11:38, 9 November 2022
Structures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APSStructures of PR1 and PR2 intermediates from time-resolved laue crystallography collected at 14ID-B, APS
Structural highlights
FunctionPYP_HALHA Photoactive blue light protein. Probably functions as a photoreceptor for a negative phototaxis response. Publication Abstract from PubMedTrans-to-cis isomerization, the key reaction in photoactive proteins, usually cannot occur through the standard one-bond-flip mechanism. Owing to spatial constraints imposed by a protein environment, isomerization probably proceeds through a volume-conserving mechanism in which highly choreographed atomic motions are expected, the details of which have not yet been observed directly. Here we employ time-resolved X-ray crystallography to visualize structurally the isomerization of the p-coumaric acid chromophore in photoactive yellow protein with a time resolution of 100 ps and a spatial resolution of 1.6 A. The structure of the earliest intermediate (I(T)) resembles a highly strained transition state in which the torsion angle is located halfway between the trans- and cis-isomers. The reaction trajectory of I(T) bifurcates into two structurally distinct cis intermediates via hula-twist and bicycle-pedal pathways. The bifurcating reaction pathways can be controlled by weakening the hydrogen bond between the chromophore and an adjacent residue through E46Q mutation, which switches off the bicycle-pedal pathway. Volume-conserving trans-cis isomerization pathways in photoactive yellow protein visualized by picosecond X-ray crystallography.,Jung YO, Lee JH, Kim J, Schmidt M, Moffat K, Srajer V, Ihee H Nat Chem. 2013 Mar;5(3):212-20. doi: 10.1038/nchem.1565. Epub 2013 Feb 3. PMID:23422563[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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